[Immunologic comparison of intracellular and extracellular serine proteases from Bacillus amyloliquefaciens and some other proteases].
Antibodies against intracellular serine protease and extracellular subtilisin BPN' were raised in rabbits. Using these antibodies and antisera against subtilisin Carlsberg and thermitase (serine protease from Thermoactinomyces vulgaris), it was shown that the proteases of the subtilisin family possess a pronounced immunological variability. Immunological studies demonstrated that the vegetative and sporulating B. amyloliquefaciens cells contain no long-lived protein precursor of intracellular serine protease and that the drastic increase of the enzyme activity during the first hours of the sporulating period is presumably due to its de novo synthesis. The specific protein inhibitor of intracellular serine protease partially purified from B. amyloliquefaciens sporulating cells did not prevent the enzyme interaction with its specific antibodies.
D000936:Antigen-Antibody Complex; D001407:Bacillus / Q000201:enzymology*; D010450:Endopeptidases / Q000276:immunology*; D007106:Immune Sera; D005779:Immunodiffusion; D007700:Kinetics; D012697:Serine Endopeptidases; D013171:Spores, Bacterial / Q000201:enzymology; D013381:Subtilisins / Q000276:immunology
D000936:Antigen-Antibody Complex; D007106:Immune Sera; D010450:Endopeptidases; D012697:Serine Endopeptidases; D013381:Subtilisins
Immunologicheskoe sravnenie vnutrikletochnoĭ i vnekletochnoĭ serinovykh proteinaz Bacillus amyloliquefaciens i nekotorykh drugikh serinovykh proteinaz.